Human LAMP-2/CD107b Alexa Fluor® 488-conjugated Antibody Summary
Leu29-Phe375
Accession # P13473
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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LAMP2/CD107b in HeLa Human Cell Line. LAMP2/CD107b was detected in formaldehyde fixed HeLa human cervical epithelial carcinoma cell line using Mouse Anti-Human LAMP2/CD107b Alexa Fluor® 488‑conjugated Monoclonal Antibody (Catalog # IC6228G) at 25 μg/mL dilution overnight at 4° C and counterstained with DAPI (blue). Specific staining was localized to lysosomes. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
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Detection of LAMP2/CD107b in HeLa Human Cell Line by Flow Cytometry. HeLa human cervical epithelial carcinoma cell line was stained with Mouse Anti-Human LAMP2/CD107b Alexa Fluor® 488-conjugated Monoclonal Antibody (Catalog # IC6228G, filled histogram) or isotype control antibody (Catalog # IC002G, open histogram). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # FC005). View our protocol for Staining Intracellular Molecules.
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Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: LAMP-2/CD107b
Lysosomal associated membrane protein 2 (LAMP2), also known as CD107b and LGP110, is an approximately 110 kDa transmembrane glycoprotein that is a major component of lysosomal membranes (1). Mature human LAMP2 consists of a 347 amino acid (aa) intralumenal domain, a 24 aa transmembrane segment, and a 35 aa cytoplasmic tail (2). Its lumenal domain is organized into two heavily N-glycosylated regions separated by a Ser/Pro-rich linker that carries a minor amount of O‑linked glycosylation (2, 3). Alternate splicing generates a human LAMP2 isoform (LAMP2B) with a substituted juxtamembrane lumenal region, transmembrane segment, and cytoplasmic tail (4). Within the lumenal domain, human LAMP2 shares approximately 64% aa sequence identity with mouse and rat LAMP2. LAMP2 itself is subject to lysosomal degradation following cleavage of its lumenal domain (5). It mediates the lysosomal uptake of the chaperone HSC73 in complex with cargo proteins and is required for the lysosomal destruction of autophagic vacuoles (6, 7). In cytotoxic T cells and mast cells, LAMP2 is expressed in the membranes of intracellular granules that contain effector molecules such as perforin, granzymes, eicosanoids, and histamine (8-10). Up‑regulated LAMP2 at the plasma membrane serves as an indicator of cell activation of CD8+ T cells, mast cells, monocytes, and platelets (9-12). LAMP2 is a native ligand for lectins Galectin-1 and Galectin-3 (13‑15).
- Eskelinen, E.-L. et al. (2003) Trends Cell Biol. 13:137.
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- Konecki, D.S. et al. (1995) Biochem. Biophys. Res. Commun. 215:757.
- Cuervo, A.M. and J.F. Dice (2000) Traffic 1:570.
- Cuervo, A.M. and J.F. Dice (1996) Science 273:501.
- Tanaka, Y. et al. (1990) Nature 406:902.
- Peters, P.J. et al. (1991) J. Exp. Med. 173:1099.
- Betts, M.R. et al. (2003) J. Immunol. Meth. 281:65.
- Grutzkau, A. et al. (2004) Cytometry 61:62.
- Kannan, K. et al. (1996) Cell. Immunol. 171:10.
- Silverstein, R.L. and M. Febbraio (1992) Blood 80:1470.
- Skrincosky, D.M. et al. (1993) Cancer Res. 53:2667.
- Inohara, H. and Raz, A. (1994) Biochem. Biophys. Res. Commun. 201:1366.
- Ohannesian D.W. et al. (1994) Cancer Res. 54:5992.
Product Datasheets
Product Specific Notices
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